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Found 15 results
Filters: keyword is MUTANT [Clear All Filters]
2008
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2008. Analysis of the thermodynamics of binding of an SH3 domain to proline-rich peptides using a chimeric fusion protein.
377(1):117-135. Abstract
2007
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2007. The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: understanding the determinants of binding affinity by comparison with Abl-SH3.
7:22. Abstract
2000
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2000. Analysis of a water mediated protein-protein interactions within RNase T1.
Biochemistry. 39(22):6586-6593. Abstract
1999
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1999. Dissection of the structural and functional role of a conserved hydration site in RNase T1.
8(4):722-730. Abstract
1998
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1998. An engineered ribonuclease preferring phosphorothioate RNA.
5(5):365-368. Abstract
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1998. Dissecting histidine interactions of ribonuclease T1 with asparagine and glutamine replacements: analysis of double mutant cycles at one position.
275(4):651-661. Abstract
1997
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1997. Additivity of protein-guanine interactions in ribonuclease T1.
272(15):9635-9639. Abstract
1996
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1996. A catalytic function for the structurally conserved residue Phe 100 of ribonuclease T1.
5(8):1523-1530. Abstract
1994
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1994. Investigation of the functional interplay between the primary site and the subsite of RNase T1: kinetic analysis of single and multiple mutants for modified substrates.
18(4):318-323. Abstract
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1994. Crystallographic study of Glu58Ala RNase T1 x 2'-guanosine monophosphate at 1.9-A resolution.
Biochemistry. 33(7):1654-1662. Abstract
1993
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1993. Functional interactions among the His40, Glu58 and His92 catalysts of ribonuclease T1 as studied by double and triple mutants.
229(3):770-781. Abstract
1992
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1992. Role of histidine-40 in ribonuclease T1 catalysis: three-dimensionalstructures of the partially active His40Lys mutant.
Biochemistry. 31(46):11317-11325. Abstract
1991
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1991. Subsite interactions of ribonuclease T1: viscosity effects indicate that the rate-limiting step of GpN transesterification depends on the nature of N.
Biochemistry. 30(35):8661-8665. Abstract
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1991. Subsite interactions of ribonuclease T1: Asn36 and Asn98 accelerate GpN transesterification through interactions with the leaving nucleoside N.
Biochemistry. 30(35):8666-8670. Abstract
1989